ID   RAM2_PETHY              Reviewed;         479 AA.
AC   A0A0M4FCN7;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase RAM2 {ECO:0000303|PubMed:25971550};
DE            EC=2.3.1.15 {ECO:0000305};
DE   AltName: Full=Protein REQUIRED FOR ARBUSCULAR MYCORRHIZATION 2 {ECO:0000303|PubMed:25971550};
GN   Name=RAM2 {ECO:0000303|PubMed:25971550};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY RAM1 AND RHIZOPHAGUS
RP   IRREGULARIS.
RC   STRAIN=cv. W138;
RX   PubMed=25971550; DOI=10.1104/pp.15.00310;
RA   Rich M.K., Schorderet M., Bapaume L., Falquet L., Morel P.,
RA   Vandenbussche M., Reinhardt D.;
RT   "The Petunia GRAS transcription factor ATA/RAM1 regulates symbiotic gene
RT   expression and fungal morphogenesis in arbuscular mycorrhiza.";
RL   Plant Physiol. 168:788-797(2015).
CC   -!- FUNCTION: Involved in the production of cutin monomers (By similarity).
CC       Esterifies acyl-group from acyl-ACP to the sn-2 position of glycerol-3-
CC       phosphate, a step in cutin biosynthesis (By similarity). Required for
CC       colonization of the root by mycorrhizal fungi, and appropriate
CC       hyphopodia and arbuscule formation (PubMed:25971550). Cutin monomers
CC       act as plant signals that promote colonization by arbuscular
CC       mycorrhizal fungi (By similarity). This signaling function has been
CC       recruited by pathogenic oomycetes to facilitate appressoria formation
CC       and their own invasion (By similarity). {ECO:0000250|UniProtKB:K7PEY4,
CC       ECO:0000269|PubMed:25971550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000305};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Regulated by RAM1 during arbuscular mycorrhiza (AM)
CC       formation after inoculation with Rhizophagus irregularis.
CC       {ECO:0000269|PubMed:25971550}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; KR612267; ALC79557.1; -; mRNA.
DR   AlphaFoldDB; A0A0M4FCN7; -.
DR   UniPathway; UPA00230; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Glycoprotein; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..479
FT                   /note="Glycerol-3-phosphate acyltransferase RAM2"
FT                   /id="PRO_0000450027"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           284..289
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:K7PEY4"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   479 AA;  52755 MW;  CFA9BA27DAF7CD89 CRC64;
     MDGTLLVGRS SFPYFALVAF EVGGIFRLLF LVLASPLAGL LYYFISESAG IRVLIFATFA
     GMKVSDIESV ARAVLPKFYS SDLHPETWHV FSSCGKRCVL TANPRIMVEG FLKEYLGADM
     VIGTEISMYK GRATGFVNKP GILVGDNKAM ALKKAFCSTS TPDIGLGDRK TDFPFMNLCK
     ESYIVRPDPG VKPMSQDKLP KPIVFHDGRL VQKPSPLMAL MIILWIPVGF LLACLRIAAG
     ALLPMPLVYY AFWALGVRVK VKGNPPPPAK KSTDQTGVLF ICSHRTLLDP IFLSTSLGRP
     IPAVTYSVSR LSEIISPIKT VRLSRDRVTD ANMIKKMLEE GDLVICPEGT TCREPFLLRF
     SALFAELTDE LVPVAMSNKM SMFHGTTARG WKGMDPFYFF MNPSPTYEVT FLNKLPYDLT
     CKAGKSSHDV ANYIQRTIAA TLSYECTNFT RKDKYKALAG NDGTVTTKPG LAAKKVMGC